Purification and properties of DNA polymerase from Mycobacterium tuberculosis H37Rv

Biochim Biophys Acta. 1981 Feb 26;652(2):274-82. doi: 10.1016/0005-2787(81)90117-9.


DNA polymerase has been purified approximately 2000-fold from Mycobacterium tuberculosis H37Rv. The purified preparation was homogeneous by electrophoretic criteria and has a molecular weight of 135 000. The purified enzyme resembles Escherichia coli polymerase I in its properties, being insensitive to sulfhydryl drugs and possessing 5',3'-exonuclease activity in addition to polymerase and 3',5'-exonuclease activities. However, it differs from the latter in its sensitivity to higher salt concentration and DNA intercalating agents such as 8-aminoquinoline. The polymerase exhibited maximal activity between 37--42 degrees C and pH 8.8--9.5. The polymerase was stable for several months below 0 degree C. However, the 5',3'-exonuclease activity was more labile. The effects of different metal ions, polyamines and drugs on the polymerase activity are presented.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • DNA-Directed DNA Polymerase / isolation & purification*
  • DNA-Directed DNA Polymerase / metabolism
  • Dactinomycin / pharmacology
  • Kinetics
  • Molecular Weight
  • Mycobacterium tuberculosis / enzymology*
  • Substrate Specificity


  • Dactinomycin
  • DNA-Directed DNA Polymerase